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  • 1
    Electronic Resource
    Electronic Resource
    Stereoselective, nonenzymic, intramolecular transfer of amino acids (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 2768-2772 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00225a005
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Catalytic roles of the AMP at the 3′ end of tRNAs (1994)
    Springer
    Molecular and cellular biochemistry 139 (1994), S. 117-121 
    Details
    ISSN: 1573-4919
    Keywords: AMP ; protein synthesis ; esterification ; peptide bond formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Recent reports suggest that the ribosome retains considerable peptidyl transferase activity even when much of the protein of the ribosome is removed and further suggests that rRNA may be the peptidyl transferase. The work here suggests that the AMP residue at the 3′ terminus of each tRNA has some catalytic activity both in the esterification reaction and in forming a pseudopeptide, AcGly, and further suggests that whatever peptidyl transferase is, it finds a cooperative substrate in the aminoacyl-AMP at the 3′ terminus of tRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01081734
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Experimental studies on the origin of the genetic code and the process of protein synthesis: A review update (1992)
    Springer
    Origins of life and evolution of the biospheres 22 (1992), S. 243-275 
    Details
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Notes: Abstract This article is an update of our earlier review (Lacey and Mullins, 1983) in this journal on the origin of the genetic code and the process of protein synthesis. It is our intent to discuss only experimental evidence published since then although there is the necessity to mention the old enough to place the new in context. We do not include theoretical nor hypothetical treatments of the code or protein synthesis. Relevant data regarding the evolution of tRNAs and the recognition of tRNAs by aminoacyl-tRNA-synthetases are discussed. Our present belief is that the code arose based on a core of early assignments which were made on a physico-chemical and anticodonic basis and this was expanded with new assignments later. These late assignments do not necessarily show an amino acid-anticodon relatedness. In spite of the fact that most data suggest a code origin based on amino acid-anticodon relationships, some new data suggesting preferential binding of Arg to its codons are discussed. While information regarding coding is not increasing very rapidly, information regarding the basic chemistry of the process of protein synthesis has increased significantly, principally relating to aminoacylation of mono- and polyribonucleotides. Included in those studies are several which show stereoselective reactions of L-amino acids with nucleotides having D-sugars. Hydrophobic interactions definitely play a role in the preferences which have been observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01810856
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Mixed anhydrides (phosphoric-carboxyl) are also formed in the esterification of 5′-amp with n-acetylaminoacyl imidazolides: Implications regarding the origin of protein synthesis (1992)
    Springer
    Origins of life and evolution of the biospheres 22 (1992), S. 361-368 
    Details
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Notes: Abstract Procedures for the formation of aminoacyl esters of monoribonucleotides with aminoacyl imidazolides were first reported by Gottikhet al. and summarized in 1970. This reaction has been widely used by us and numbers of other workers as a convenient means of preparing aminoacyl esters of nucleotides. We have previously reported that, under conditions of excess imidazolide, large amounts of bis 2′, 3′ esters are formed in addition to the monoesters, (Laceyet al., 1991). However, to our knowledge, no one has reported that in addition to the esters, relatively large amounts of the mixed anhydride, with the amino acid carboxyl attached to the phosphate, are also formed at short reaction times. We report here on the relative amounts of anhydride and esters formed in this reaction of racemic mixtures of eleven N-acetyl amino acid imidazolides with 5′-AMP and discuss the relevance of the findings to the origin of protein synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01809372
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  • 5
    Electronic Resource
    Electronic Resource
    N-Acetyl-D and L-esters of 5′-AMP hydrolyze at different rates (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 5 (1993), S. 150-153 
    Details
    ISSN: 0899-0042
    Keywords: aminoacyl adenylate esters ; hydrolytic stabilization by intramolecular interaction ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Studies of the properties of aminoacyl derivatives of 5′-AMP are aimed at understanding the origin of the process of protein synthesis. Aminoacyl (2′,3′) esters of 5′-AMP can serve as models of the 3′-terminus of aminoacyl tRNA. We report here on the relative rates of hydrolysis of AC-D- and L-Phe AMP esters as a function of pH. At all pHs above 3, the rate constant of hydrolysis of the AC-L-Phe ester is 1.7 to 2.1 times that of AC-D-Phe ester. The D-isomer seems partially protected from hydrolysis by a stronger association with the adenine ring of the 5′-AMP. © 1993 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chir.530050308
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    Paper (German National Licenses)
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